SBIR1_ARATH
ID SBIR1_ARATH Reviewed; 641 AA.
AC Q9SKB2; Q93Z40;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1;
DE EC=2.7.10.1;
DE EC=2.7.11.1;
DE AltName: Full=Protein EVERSHED;
DE AltName: Full=Protein SUPPRESSOR OF BIR1-1;
DE Flags: Precursor;
GN Name=SOBIR1; Synonyms=EVR; OrderedLocusNames=At2g31880; ORFNames=F20M17.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-129; SER-329;
RP GLY-356; ARG-417; ASN-455; GLY-557; GLU-575 AND ARG-626.
RX PubMed=19616764; DOI=10.1016/j.chom.2009.05.019;
RA Gao M., Wang X., Wang D., Xu F., Ding X., Zhang Z., Bi D., Cheng Y.T.,
RA Chen S., Li X., Zhang Y.;
RT "Regulation of cell death and innate immunity by two receptor-like kinases
RT in Arabidopsis.";
RL Cell Host Microbe 6:34-44(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF LYS-377 AND GLU-407.
RX PubMed=20081191; DOI=10.1242/dev.041335;
RA Leslie M.E., Lewis M.W., Youn J.-Y., Daniels M.J., Liljegren S.J.;
RT "The EVERSHED receptor-like kinase modulates floral organ shedding in
RT Arabidopsis.";
RL Development 137:467-476(2010).
RN [8]
RP INTERACTION WITH CST.
RX PubMed=21628627; DOI=10.1104/pp.111.175224;
RA Burr C.A., Leslie M.E., Orlowski S.K., Chen I., Wright C.E., Daniels M.J.,
RA Liljegren S.J.;
RT "CAST AWAY, a membrane-associated receptor-like kinase, inhibits organ
RT abscission in Arabidopsis.";
RL Plant Physiol. 156:1837-1850(2011).
RN [9]
RP REVIEW.
RX PubMed=25064074; DOI=10.1016/j.pbi.2014.07.007;
RA Gust A.A., Felix G.;
RT "Receptor like proteins associate with SOBIR1-type of adaptors to form
RT bimolecular receptor kinases.";
RL Curr. Opin. Plant Biol. 21:104-111(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RLP23.
RX PubMed=24525519; DOI=10.4161/psb.27937;
RA Bi G., Liebrand T.W., Cordewener J.H., America A.H., Xu X., Joosten M.H.;
RT "Arabidopsis thaliana receptor-like protein AtRLP23 associates with the
RT receptor-like kinase AtSOBIR1.";
RL Plant Signal. Behav. 9:E27937-E27937(2014).
RN [11]
RP FUNCTION, SUBUNIT, AND COMPONENT OF THE RLP23-SOBIR1-BAK1 COMPLEX.
RX PubMed=27251392; DOI=10.1038/nplants.2015.140;
RA Albert I., Boehm H., Albert M., Feiler C.E., Imkampe J., Wallmeroth N.,
RA Brancato C., Raaymakers T.M., Oome S., Zhang H., Krol E., Grefen C.,
RA Gust A.A., Chai J., Hedrich R., Van den Ackerveken G., Nuernberger T.;
RT "An RLP23-SOBIR1-BAK1 complex mediates NLP-triggered immunity.";
RL Nat. Plants 1:15140-15140(2015).
CC -!- FUNCTION: Dual specificity kinase acting on both serine/threonine- and
CC tyrosine-containing substrates. Acting as a counterplayer of BIR1,
CC promotes the activation of plant defense and cell death
CC (PubMed:19616764). Component of the RLP23-SOBIR1-BAK1 complex that
CC mediates NLP-triggered immunity (PubMed:27251392). Functions as an
CC inhibitor/regulator of abscission, probably by regulating membrane
CC trafficking during abscission (PubMed:20081191).
CC {ECO:0000269|PubMed:19616764, ECO:0000269|PubMed:20081191,
CC ECO:0000269|PubMed:27251392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:20081191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20081191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027,
CC ECO:0000269|PubMed:20081191};
CC -!- SUBUNIT: Interacts with CST (PubMed:21628627). Interacts with RLP23
CC (PubMed:24525519, PubMed:27251392). Component of a trimeric complex
CC composed of RLP23, SOBIR1 and BAK1. BAK1 is recruited into a pre-formed
CC RLP23-SOBIR1 complex in a ligand-dependent manner (PubMed:27251392).
CC {ECO:0000269|PubMed:21628627, ECO:0000269|PubMed:24525519,
CC ECO:0000269|PubMed:27251392}.
CC -!- INTERACTION:
CC Q9SKB2; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-16905883, EBI-20651385;
CC Q9SKB2; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-16905883, EBI-1238661;
CC Q9SKB2; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16905883, EBI-20651541;
CC Q9SKB2; A0A1I9LQ53: At3g50230; NbExp=3; IntAct=EBI-16905883, EBI-20654045;
CC Q9SKB2; C0LGR9: At4g31250; NbExp=2; IntAct=EBI-16905883, EBI-16955262;
CC Q9SKB2; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-16905883, EBI-16905069;
CC Q9SKB2; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-16905883, EBI-16914444;
CC Q9SKB2; Q9LVI6: RLK902; NbExp=3; IntAct=EBI-16905883, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20081191,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:20081191, ECO:0000305|PubMed:17644812}.
CC -!- TISSUE SPECIFICITY: Mostly present in leaves and flowers, with
CC increasing expression in older flowers. {ECO:0000269|PubMed:20081191}.
CC -!- DEVELOPMENTAL STAGE: Expressed in floral organ abscission zones (AZs)
CC prior to cell separation and subsequent shedding. Also present within
CC the style of developing fruits, at the bases of cauline leaves, and in
CC the stems of the first rosette leaves. {ECO:0000269|PubMed:20081191}.
CC -!- PTM: Autophosphorylated on Ser, Thr and Tyr residues.
CC -!- DISRUPTION PHENOTYPE: Suppresses BIR1 (bir1-1) disruption phenotype.
CC When associated with AGD5/NEV disruption, premature shedding of floral
CC organs and enlarge abscission zones. {ECO:0000269|PubMed:19616764,
CC ECO:0000269|PubMed:20081191}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC006533; AAD32284.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08599.1; -; Genomic_DNA.
DR EMBL; AF370596; AAK43915.1; -; mRNA.
DR EMBL; AY058153; AAL25569.1; -; mRNA.
DR EMBL; FJ708707; ACN59302.1; -; mRNA.
DR PIR; C84726; C84726.
DR RefSeq; NP_180747.1; NM_128746.3.
DR PDB; 6R1H; X-ray; 1.55 A; A/B=1-270.
DR PDBsum; 6R1H; -.
DR AlphaFoldDB; Q9SKB2; -.
DR SMR; Q9SKB2; -.
DR BioGRID; 3093; 64.
DR IntAct; Q9SKB2; 61.
DR STRING; 3702.AT2G31880.1; -.
DR iPTMnet; Q9SKB2; -.
DR SwissPalm; Q9SKB2; -.
DR PaxDb; Q9SKB2; -.
DR PRIDE; Q9SKB2; -.
DR ProteomicsDB; 228132; -.
DR EnsemblPlants; AT2G31880.1; AT2G31880.1; AT2G31880.
DR GeneID; 817746; -.
DR Gramene; AT2G31880.1; AT2G31880.1; AT2G31880.
DR KEGG; ath:AT2G31880; -.
DR Araport; AT2G31880; -.
DR TAIR; locus:2045228; AT2G31880.
DR eggNOG; ENOG502QW02; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9SKB2; -.
DR OMA; SRPECHY; -.
DR OrthoDB; 468106at2759; -.
DR PhylomeDB; Q9SKB2; -.
DR PRO; PR:Q9SKB2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKB2; baseline and differential.
DR Genevisible; Q9SKB2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0060862; P:negative regulation of floral organ abscission; IGI:TAIR.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:TAIR.
DR GO; GO:0031349; P:positive regulation of defense response; IMP:TAIR.
DR DisProt; DP02660; -.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..641
FT /note="Leucine-rich repeat receptor-like
FT serine/threonine/tyrosine-protein kinase SOBIR1"
FT /id="PRO_0000403355"
FT TOPO_DOM 32..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 112..133
FT /note="LRR 1"
FT REPEAT 136..159
FT /note="LRR 2"
FT REPEAT 160..182
FT /note="LRR 3"
FT REPEAT 183..205
FT /note="LRR 4"
FT REPEAT 207..228
FT /note="LRR 5"
FT DOMAIN 347..641
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 243..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 353..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 129
FT /note="V->M: In sobir1-8; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 329
FT /note="S->N: In sobir1-4; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 356
FT /note="G->R: In sobir1-7; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 377
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:20081191"
FT MUTAGEN 407
FT /note="E->K: In evr-2; loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:20081191"
FT MUTAGEN 417
FT /note="R->W: In sobir1-9; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 455
FT /note="N->D: In sobir1-10; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 557
FT /note="G->R: In sobir1-5; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 575
FT /note="E->K: In sobir1-2; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT MUTAGEN 626
FT /note="R->K: In sobir1-6; suppresses BIR1 (bir1-1)
FT disruption phenotype."
FT /evidence="ECO:0000269|PubMed:19616764"
FT CONFLICT 112
FT /note="E -> V (in Ref. 3; AAL25569)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="L -> S (in Ref. 3; AAL25569)"
FT /evidence="ECO:0000305"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:6R1H"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6R1H"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6R1H"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6R1H"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6R1H"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:6R1H"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6R1H"
SQ SEQUENCE 641 AA; 71111 MW; C061139D4B52681C CRC64;
MAVPTGSANL FLRPLILAVL SFLLLSSFVS SVEWLDIDSS DLKALQVIET ELGVNSQRSS
ASDVNPCGRR GVFCERRHSA TTGEYVLRVT RLVYRSRSLT GTISPVIGML SELKELTLSN
NQLVNAVPVD ILSCKQLEVL DLRKNRFSGQ IPGNFSSLSR LRILDLSSNK LSGNLNFLKN
LRNLENLSVA NNLFSGKIPE QIVSFHNLRF FDFSGNRYLE GPAPVMSSIK LQTSPHQTRH
ILAETPTSSP TNKPNNSTTS KAPKGAPKPG KLKKKKKKSK KKKVAAWILG FVVGAIGGTI
SGFVFSVLFK LIIQAIRGSE KPPGPSIFSP LIKKAEDLAF LENEEALASL EIIGRGGCGE
VFKAELPGSN GKIIAVKKVI QPPKDADELT DEDSKFLNKK MRQIRSEINT VGHIRHRNLL
PLLAHVSRPE CHYLVYEYME KGSLQDILTD VQAGNQELMW PARHKIALGI AAGLEYLHMD
HNPRIIHRDL KPANVLLDDD MEARISDFGL AKAMPDAVTH ITTSHVAGTV GYIAPEFYQT
HKFTDKCDIY SFGVILGILV IGKLPSDEFF QHTDEMSLIK WMRNIITSEN PSLAIDPKLM
DQGFDEQMLL VLKIACYCTL DDPKQRPNSK DVRTMLSQIK H
